TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis
AU - Goyal, Aneesh
AU - Yousuf, Malikmohamed
AU - Rajakumara, Eerappa
AU - Arora, Pooja
AU - Gokhale, Rajesh S.
AU - Sankaranarayanan, Rajan
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2006/4
Y1 - 2006/4
N2 - FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P212121, with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 Å. The crystal structure of the N-terminal domain of FadD28 at 2.35 Å resolution has been solved using the MAD method.
AB - FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P212121, with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 Å. The crystal structure of the N-terminal domain of FadD28 at 2.35 Å resolution has been solved using the MAD method.
UR - http://www.scopus.com/inward/record.url?scp=33645762737&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33645762737&partnerID=8YFLogxK
U2 - 10.1107/S1744309106005938
DO - 10.1107/S1744309106005938
M3 - Article
C2 - 16582482
AN - SCOPUS:33645762737
SN - 1744-3091
VL - 62
SP - 350
EP - 352
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 4
ER -